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- Title
Modulation of the competition between renaturation and aggregation of lysozyme by additive mixtures.
- Authors
Takalloo, Zeinab; Niknaddaf, Forouzan; Shahangian, S. Shirin; Heydari, Akbar; Hosseinkhani, Saman; H. Sajedi, Reza
- Abstract
The effects of 17 kinds of additive mixtures have been studied on refolding and aggregation of a model protein, lysozyme. Most of the prepared mixtures were efficient in inhibiting aggregation of the protein, and, surprisingly, four novel additive mixtures, i.e., lactic acid: l‐arginine, lactic acid: l‐glutamine, choline chloride: lactic acid, and imidazolium salt: β‐cyclodextrin as well as choline chloride: urea exhibited a more remarkable efficacy in suppressing aggregation. Among these, lactic acid: l‐arginine was identified as the most efficient additive, and lactic acid: l‐glutamine and choline chloride: lactic acid were inefficient to recover the enzyme activity. In contrast, choline chloride: ethylene glycol: imidazole, choline chloride: glycerol: imidazole, imidazole: betaine: ethylene glycol were found to be less effective mixtures in preventing enzyme aggregation. Totally, it was demonstrated that the protective effects of the mixtures were improved as their concentrations increased. The improvement was more remarkable for imidazolium salt: β‐cyclodextrin and choline chloride: urea, where the denatured lysozyme was reactivated and recovered up to 85% of its initial activity by enhancing their concentrations from 1 to 5% (V/V). It is suggested that such solution additives may be further employed as artificial chaperones to assist protein folding and stability.
- Subjects
CHOLINE chloride; GLUTAMINE; LYSOZYMES; LACTIC acid; MOLECULAR chaperones; MIXTURES; ETHYLENE glycol; PROTEIN stability
- Publication
Biotechnology & Applied Biochemistry, 2020, Vol 67, Issue 3, p330
- ISSN
0885-4513
- Publication type
Article
- DOI
10.1002/bab.1864